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Conserved domains on  [gi|502824006|ref|WP_013058982|]
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MULTISPECIES: pantetheine-phosphate adenylyltransferase [Bacillaceae]

Protein Classification

pantetheine-phosphate adenylyltransferase( domain architecture ID 10786277)

pantetheine-phosphate adenylyltransferase catalyzes the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) to form dephospho-CoA (dPCoA) and pyrophosphate in the Coenzyme A (CoA) biosynthetic pathway

CATH:  3.40.50.620
EC:  2.7.7.3
Gene Ontology:  GO:0005524|GO:0015937|GO:0004595
PubMed:  33271445

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 4-160 7.78e-103

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


:

Pssm-ID: 440433  Cd Length: 159  Bit Score: 291.52  E-value: 7.78e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006   4 IAVCPGSFDPVTNGHFDIIKRGANVFDTIYVVVLNNSSKSPLFTGEERVALLKEVTKSLPNVVVESYSGLLMEYAKEKQA 83
Cdd:COG0669    3 IAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREVGA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502824006  84 KTILRGLRAVSDFEYEMQITSVNRVLDKEIETLFMMTNNQYSFLSSSIVKEVAKYGGNISELVPPPVREALAEKFEQ 160
Cdd:COG0669   83 NVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 4-160 7.78e-103

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440433  Cd Length: 159  Bit Score: 291.52  E-value: 7.78e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006   4 IAVCPGSFDPVTNGHFDIIKRGANVFDTIYVVVLNNSSKSPLFTGEERVALLKEVTKSLPNVVVESYSGLLMEYAKEKQA 83
Cdd:COG0669    3 IAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREVGA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502824006  84 KTILRGLRAVSDFEYEMQITSVNRVLDKEIETLFMMTNNQYSFLSSSIVKEVAKYGGNISELVPPPVREALAEKFEQ 160
Cdd:COG0669   83 NVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 4-156 6.20e-92

Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli.


Pssm-ID: 173914 [Multi-domain]  Cd Length: 153  Bit Score: 263.56  E-value: 6.20e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006   4 IAVCPGSFDPVTNGHFDIIKRGANVFDTIYVVVLNNSSKSPLFTGEERVALLKEVTKSLPNVVVESYSGLLMEYAKEKQA 83
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502824006  84 KTILRGLRAVSDFEYEMQITSVNRVLDKEIETLFMMTNNQYSFLSSSIVKEVAKYGGNISELVPPPVREALAE 156
Cdd:cd02163   81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 4-158 1.08e-74

pantetheine-phosphate adenylyltransferase, bacterial; This model describes pantetheine-phosphate adenylyltransferase, the penultimate enzyme of coenzyme A (CoA) biosynthesis in bacteria. It does not show any strong homology to eukaryotic enzymes of coenzyme A biosynthesis. This protein was previously designated KdtB and postulated (because of cytidyltransferase homology and proximity to kdtA) to be an enzyme of LPS biosynthesis, a cytidyltransferase for 3-deoxy-D-manno-2-octulosonic acid. However, no activity toward that compound was found with either CTP or ATP. The phylogenetic distribution of this enzyme is more consistent with coenzyme A biosynthesis than with LPS biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273663 [Multi-domain]  Cd Length: 155  Bit Score: 220.22  E-value: 1.08e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006    4 IAVCPGSFDPVTNGHFDIIKRGANVFDTIYVVVLNNSSKSPLFTGEERVALLKEVTKSLPNVVVESYSGLLMEYAKEKQA 83
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502824006   84 KTILRGLRAVSDFEYEMQITSVNRVLDKEIETLFMMTNNQYSFLSSSIVKEVAKYGGNISELVPPPVREALAEKF 158
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 6-135 5.63e-27

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 98.55  E-value: 5.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006    6 VCPGSFDPVTNGHFDIIKRGANVFD-TIYVVVLNNSS----KSPLFTGEERVALLKEVtKSLPNVVVESYSGLLMEYAKE 80
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDeDLIVGVPSDEPphklKRPLFSAEERLEMLELA-KWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 502824006   81 KQAKTILRGLRAVSDFEYEMQITSVNRVLDKEIETLFMMTNNQYSFLSSSIVKEV 135
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
4-70 1.04e-05

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 44.17  E-value: 1.04e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502824006   4 IAVCPGSFDPVTNGHFDIIKRGANV--FDTIYVVVLNNS---SKSPLFTGEERVALLKEVTKSLPNVVVESY 70
Cdd:PRK07152   3 IAIFGGSFDPIHKGHINIAKKAIKKlkLDKLFFVPTYINpfkKKQKASNGEHRLNMLKLALKNLPKMEVSDF 74
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
 13-78 8.84e-05

Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain of citrate lyase ligase EC:6.2.1.22.


Pssm-ID: 129003  Cd Length: 182  Bit Score: 40.69  E-value: 8.84e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502824006    13 PVTNGHFDIIKRGANVFDTIYVVVLNNSSKspLFTGEERVALLKEVTKSLPNVVVESYSGLLMEYA 78
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVHLFVVSEDAS--LFSFDERFALVKKGTKDLDNVTVHSGSDYIISRA 73
 
Name Accession Description Interval E-value
CoaD COG0669
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ...
 4-160 7.78e-103

Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 440433  Cd Length: 159  Bit Score: 291.52  E-value: 7.78e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006   4 IAVCPGSFDPVTNGHFDIIKRGANVFDTIYVVVLNNSSKSPLFTGEERVALLKEVTKSLPNVVVESYSGLLMEYAKEKQA 83
Cdd:COG0669    3 IAVYPGSFDPITNGHLDIIERAAKLFDEVIVAVAVNPSKKPLFSLEERVELIREALADLPNVEVDSFDGLLVDFAREVGA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502824006  84 KTILRGLRAVSDFEYEMQITSVNRVLDKEIETLFMMTNNQYSFLSSSIVKEVAKYGGNISELVPPPVREALAEKFEQ 160
Cdd:COG0669   83 NVIVRGLRAVSDFEYEFQMALMNRKLAPEIETVFLMTSPEYSFISSSLVKEIARLGGDVSGFVPPAVAEALKEKFAK 159
PPAT cd02163
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ...
 4-156 6.20e-92

Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli.


Pssm-ID: 173914 [Multi-domain]  Cd Length: 153  Bit Score: 263.56  E-value: 6.20e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006   4 IAVCPGSFDPVTNGHFDIIKRGANVFDTIYVVVLNNSSKSPLFTGEERVALLKEVTKSLPNVVVESYSGLLMEYAKEKQA 83
Cdd:cd02163    1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAVAVNPSKKPLFSLEERVELIREATKHLPNVEVDGFDGLLVDFARKHGA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502824006  84 KTILRGLRAVSDFEYEMQITSVNRVLDKEIETLFMMTNNQYSFLSSSIVKEVAKYGGNISELVPPPVREALAE 156
Cdd:cd02163   81 NVIVRGLRAVSDFEYEFQMAGMNRKLAPEIETVFLMASPEYSFISSSLVKEIARFGGDVSGFVPPVVAKALKE 153
coaD_prev_kdtB TIGR01510
pantetheine-phosphate adenylyltransferase, bacterial; This model describes ...
 4-158 1.08e-74

pantetheine-phosphate adenylyltransferase, bacterial; This model describes pantetheine-phosphate adenylyltransferase, the penultimate enzyme of coenzyme A (CoA) biosynthesis in bacteria. It does not show any strong homology to eukaryotic enzymes of coenzyme A biosynthesis. This protein was previously designated KdtB and postulated (because of cytidyltransferase homology and proximity to kdtA) to be an enzyme of LPS biosynthesis, a cytidyltransferase for 3-deoxy-D-manno-2-octulosonic acid. However, no activity toward that compound was found with either CTP or ATP. The phylogenetic distribution of this enzyme is more consistent with coenzyme A biosynthesis than with LPS biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 273663 [Multi-domain]  Cd Length: 155  Bit Score: 220.22  E-value: 1.08e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006    4 IAVCPGSFDPVTNGHFDIIKRGANVFDTIYVVVLNNSSKSPLFTGEERVALLKEVTKSLPNVVVESYSGLLMEYAKEKQA 83
Cdd:TIGR01510   1 IALYPGSFDPVTNGHLDIIKRAAALFDEVIVAVAKNPSKKPLFSLEERVELIKDATKHLPNVRVDVFDGLLVDYAKELGA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502824006   84 KTILRGLRAVSDFEYEMQITSVNRVLDKEIETLFMMTNNQYSFLSSSIVKEVAKYGGNISELVPPPVREALAEKF 158
Cdd:TIGR01510  81 TFIVRGLRAATDFEYELQMALMNKHLAPEIETVFLMASPEYAFVSSSLVKEIASFGGDVSNLVPPAVARRLKAKF 155
CTP_transf_like pfam01467
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ...
 6-135 5.63e-27

Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases.


Pssm-ID: 396172 [Multi-domain]  Cd Length: 134  Bit Score: 98.55  E-value: 5.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006    6 VCPGSFDPVTNGHFDIIKRGANVFD-TIYVVVLNNSS----KSPLFTGEERVALLKEVtKSLPNVVVESYSGLLMEYAKE 80
Cdd:pfam01467   1 LFGGTFDPIHLGHLRLLEQAKELFDeDLIVGVPSDEPphklKRPLFSAEERLEMLELA-KWVDEVIVVAPWELTRELLKE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 502824006   81 KQAKTILRGLRAVSDFEYEMQITSVNRVLDKEIETLFMMTNNQYSFLSSSIVKEV 135
Cdd:pfam01467  80 LNPDVLVIGADSLLDFWYELDEILGNVKLVVVVRPVFFIPLKPTNGISSTDIRER 134
cyt_tran_rel TIGR00125
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ...
 4-64 2.66e-15

cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.


Pssm-ID: 272920 [Multi-domain]  Cd Length: 66  Bit Score: 66.56  E-value: 2.66e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502824006    4 IAVCPGSFDPVTNGHFDIIKRGANVFDTIYVVVL-----NNSSKSPLFTGEERVALLKEVTKSLPN 64
Cdd:TIGR00125   1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGsdqfvNPLKGEPVFSLEERLEMLKALKYVDEV 66
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 4-134 2.41e-09

Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.


Pssm-ID: 185678 [Multi-domain]  Cd Length: 143  Bit Score: 52.83  E-value: 2.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006   4 IAVCPGSFDPVTNGHFDIIKRGANVFDTIYVVVLNNSSKSP-----LFTGEERVALLKEVTKSLPNVVV-------ESYS 71
Cdd:cd02039    1 VGIIIGRFEPFHLGHLKLIKEALEEALDEVIIIIVSNPPKKkrnkdPFSLHERVEMLKEILKDRLKVVPvdfpevkILLA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502824006  72 GL-LMEYAKEKQAKTILRGLRAVSDFEYEMQITSVNRVLDKEIETLFMMTNNQysFLSSSIVKE 134
Cdd:cd02039   81 VVfILKILLKVGPDKVVVGEDFAFGKNASYNKDLKELFLDIEIVEVPRVRDGK--KISSTLIRE 142
NMNAT cd02165
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ...
 4-152 4.56e-09

Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis.


Pssm-ID: 185680 [Multi-domain]  Cd Length: 192  Bit Score: 53.01  E-value: 4.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006   4 IAVCPGSFDPVTNGHFDIIKRGANVF--DTIYVVVLNNS--SKSPLFTGEERVALLKEVTKSLPNVVVE---------SY 70
Cdd:cd02165    1 IALFGGSFDPPHLGHLAIAEEALEELglDRVLLLPSANPphKPPKPASFEHRLEMLKLAIEDNPKFEVSdieikrdgpSY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006  71 SGLLMEYAKE----------------------KQAKTILRGLRAV----SDFEYEMQITSVNRVLDKEIETLFMMTNNqy 124
Cdd:cd02165   81 TIDTLEELRErypnaelyfiigsdnlirlpkwYDWEELLSLVHLVvaprPGYPIEDASLEKLLLPGGRIILLDNPLLN-- 158

                        170       180
                 ....*....|....*....|....*...
gi 502824006 125 sfLSSSIVKEVAKYGGNISELVPPPVRE 152
Cdd:cd02165  159 --ISSTEIRERLKNGKSIRYLLPPAVAD 184
TIGR00482 TIGR00482
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ...
 9-152 1.96e-07

nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the predominant bacterial/eukaryotic adenylyltransferase for nicotinamide-nucleotide, its deamido form nicotinate nucleotide, or both. The first activity, nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1), synthesizes NAD by the salvage pathway, while the second, nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) synthesizes the immediate precursor of NAD by the de novo pathway. In E. coli, NadD activity is biased toward the de novo pathway while salvage activity is channeled through the multifunctional NadR protein, but this division of labor may be exceptional. The given name of this model, nicotinate (nicotinamide) nucleotide adenylyltransferase, reflects the lack of absolute specificity with respect to substrate amidation state in most species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273101 [Multi-domain]  Cd Length: 193  Bit Score: 48.47  E-value: 1.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006    9 GSFDPVTNGHFDIIKRGANVFDT--IYVVVLNNSSKSPLFTG---EERVALLKEVTKSLPNVVVE---------SYSGLL 74
Cdd:TIGR00482   4 GSFDPIHYGHLLLAEEALDHLDLdkVIFVPTANPPHKKTYEAassHHRLAMLKLAIEDNPKFEVDdfeikrggpSYTIDT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006   75 MEYAKEKQAKT---ILRGLRAVSDFE----YEM-----QITSVNRV------LDKEIETLFMMTNNQYSF------LSSS 130
Cdd:TIGR00482  84 LKHLKKKYPDVelyFIIGADALRSFPlwkdWQEllelvHLVIVPRPgytldkALLEKAILRMHHGNLTLLhnprvpISST 163

                         170       180
                  ....*....|....*....|..
gi 502824006  131 IVKEVAKYGGNISELVPPPVRE 152
Cdd:TIGR00482 164 EIRQRIRQGKSIEYLLPDPVIK 185
NadD COG1057
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ...
 1-157 1.23e-06

Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; Nicotinate-nucleotide adenylyltransferase NadD is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 440677 [Multi-domain]  Cd Length: 197  Bit Score: 46.27  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006   1 MGSIAVCPGSFDPVTNGHFDIIKRGANVF--DTIYVVVLNNS---SKSPLFTGEERVALLKEVTKSLPNVVVE------- 68
Cdd:COG1057    1 MMRIGIFGGTFDPIHIGHLALAEEAAEQLglDEVIFVPAGQPphkKHKPLASAEHRLAMLRLAIADNPRFEVSdielerp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006  69 --SYSGLLMEYAKEKQAKT----ILrGLRAVSDF----EYEmQITS------VNR---VLDKEIETLFMMTNNQYSFL-- 127
Cdd:COG1057   81 gpSYTIDTLRELREEYPDAelyfII-GADALLQLpkwkRWE-ELLElahlvvVPRpgyELDELEELEALKPGGRIILLdv 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 502824006 128 -----SSSIVKEVAKYGGNISELVPPPVREALAEK 157
Cdd:COG1057  159 plldiSSTEIRERLAEGKSIRYLVPDAVEDYIREH 193
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
4-70 1.04e-05

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 44.17  E-value: 1.04e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502824006   4 IAVCPGSFDPVTNGHFDIIKRGANV--FDTIYVVVLNNS---SKSPLFTGEERVALLKEVTKSLPNVVVESY 70
Cdd:PRK07152   3 IAIFGGSFDPIHKGHINIAKKAIKKlkLDKLFFVPTYINpfkKKQKASNGEHRLNMLKLALKNLPKMEVSDF 74
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 5-130 1.98e-05

nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.


Pssm-ID: 173912 [Multi-domain]  Cd Length: 105  Bit Score: 41.37  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824006   5 AVCPGSFDPVTNGHFDIIKRGANVFDTIYVVVLNNS---SKSPLFTGEERVALLKEvtkslpnvvvesysgllmeyakek 81
Cdd:cd02156    2 ARFPGEPGYLHIGHAKLICRAKGIADQCVVRIDDNPpvkVWQDPHELEERKESIEE------------------------ 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 502824006  82 qaKTILRGLRAVSDFEYEMQITSvNRVLDKEIETLFM-MTNNQYSFLSSS 130
Cdd:cd02156   58 --DISVCGEDFQQNRELYRWVKD-NITLPVDPEQVELpRLNLETTVMSKR 104
Citrate_lyase_ligase cd02169
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ...
 13-78 8.70e-05

Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is responsible for acetylation of the (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) prosthetic group of the gamma subunit of citrate lyase, converting the inactive thiol form of this enzyme to the active form. The acetylation of 1 molecule of deacetyl-citrate lyase to enzymatically active citrate lyase requires 6 molecules of ATP. The Adenylylyltranferase activity of the enzyme involves the formation of AMP and and pyrophosphate in the acetylation reaction.


Pssm-ID: 173920 [Multi-domain]  Cd Length: 297  Bit Score: 41.48  E-value: 8.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502824006  13 PVTNGHFDIIKRGANVFDTIYVVVLNNSSKspLFTGEERVALLKEVTKSLPNVVVESYSGLLMEYA 78
Cdd:cd02169  125 PFTLGHRYLVEKAAAENDWVHLFVVSEDKS--LFSFADRFKLVKKGTKHLKNVTVHSGGDYIISSA 188
Citrate_ly_lig smart00764
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ...
 13-78 8.84e-05

Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain of citrate lyase ligase EC:6.2.1.22.


Pssm-ID: 129003  Cd Length: 182  Bit Score: 40.69  E-value: 8.84e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502824006    13 PVTNGHFDIIKRGANVFDTIYVVVLNNSSKspLFTGEERVALLKEVTKSLPNVVVESYSGLLMEYA 78
Cdd:smart00764  10 PFTLGHRYLVEQAAAECDWVHLFVVSEDAS--LFSFDERFALVKKGTKDLDNVTVHSGSDYIISRA 73
nadD PRK00071
nicotinate-nucleotide adenylyltransferase;
1-68 4.92e-04

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 234611 [Multi-domain]  Cd Length: 203  Bit Score: 38.66  E-value: 4.92e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502824006   1 MGSIAVCPGSFDPVTNGHFDIIKRGANVFD---TIYVVVLNNS--SKSPLFTGEERVALLKEVTKSLPNVVVE 68
Cdd:PRK00071   3 MKRIGLFGGTFDPPHYGHLAIAEEAAERLGldeVWFLPNPGPPhkPQKPLAPLEHRLAMLELAIADNPRFSVS 75
cytidylyltransferase cd02170
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ...
 6-64 2.15e-03

cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate cytidylyltransferase (CCT), glycerol-3-phosphate cytidylyltransferase, RafE and phosphoethanolamine cytidylyltransferase (ECT). All enzymes catalyze the transfer of a cytidylyl group from CTP to various substrates.


Pssm-ID: 173921 [Multi-domain]  Cd Length: 136  Bit Score: 36.50  E-value: 2.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502824006   6 VCPGSFDPVTNGHFDIIKRGANVFDTIYVVVLNNSS-----KSPLFTGEER---VALLKEVTKSLPN 64
Cdd:cd02170    5 YAAGTFDIIHPGHIRFLEEAKKLGDYLIVGVARDETvakikRRPILPEEQRaevVEALKYVDEVILG 71
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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